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Science 29 October 2004:
Vol. 306. no. 5697, pp. 818 - 820
DOI: 10.1126/science.1105457
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Perspectives

BIOCHEMISTRY:
How Active Sites Communicate in Thiamine Enzymes

Frank Jordan

Thiamine enzymes require thiamine in its diphosphate form as a cofactor. In his Perspective, Jordan discusses a new study that highlights how the active sites of thiamine enzymes communicate (Frank et al.).

The author is in the Department of Chemistry, Rutgers University, Newark, NJ 07102, USA. E-mail: frjordan{at}newark.rutgers.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Conformational Ensemble Modulates Cooperativity in the Rate-determining Catalytic Step in the E1 Component of the Escherichia coli Pyruvate Dehydrogenase Multienzyme Complex.
S. Kale and F. Jordan (2009)
J. Biol. Chem. 284, 33122-33129
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Science. ISSN 0036-8075 (print), 1095-9203 (online)